ID   7OMT6_MEDSA             Reviewed;         352 AA.
AC   O22308;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Isoflavone-7-O-methyltransferase 6;
DE            EC=2.1.1.150;
DE   AltName: Full=7-IOMT-6;
DE   AltName: Full=Isoflavone-O-methyltransferase 6;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9484461; DOI=10.1023/a:1005938121453;
RA   He X.-Z., Reddy J.T., Dixon R.A.;
RT   "Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning and
RT   characterization of an elicitor-inducible isoflavone 7-O-
RT   methyltransferase.";
RL   Plant Mol. Biol. 36:43-54(1998).
CC   -!- FUNCTION: Transfers a methyl group to 7-hydroxyls of the isoflavones
CC       daidzein, genistein and 6,7,4'-trihydroxyisoflavone. Can also methylate
CC       (+)6a-hydroxymaackiain with lower efficiency.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 7-hydroxyisoflavone + S-adenosyl-L-methionine = a 7-
CC         methoxyisoflavone + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:17933, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:140356;
CC         EC=2.1.1.150;
CC   -!- PATHWAY: Phytoalexin biosynthesis; medicarpin biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; AF000975; AAC49926.1; -; mRNA.
DR   AlphaFoldDB; O22308; -.
DR   SMR; O22308; -.
DR   KEGG; ag:AAC49926; -.
DR   UniPathway; UPA00902; -.
DR   GO; GO:0033800; F:isoflavone 7-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..352
FT                   /note="Isoflavone-7-O-methyltransferase 6"
FT                   /id="PRO_0000204436"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT   BINDING         118..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         219
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   352 AA;  39605 MW;  31B95226966C1C98 CRC64;
     MASSINGRKP SEIFKAQALL YKHIYAFIDS MSLKWAVEMN IPNIIQNHGK PISLSNLVSI
     LQVPSSKIGN VRRLMRYLAH NGFFEIITKE EESYALTVAS ELLVRGSDLC LAPMVECVLD
     PTLSGSYHEL KKWIYEEDLT LFGVTLGSGF WDFLDKNPEY NTSFNDAMAS DSKLINLALR
     DCDFVFDGLE SIVDVGGGTG TTAKIICETF PKLKCIVFDR PQVVENLSGS NNLTYVGGDM
     FTSIPNADAV LLKYILHNWT DKDCLRILKK CKEAVTNDGK RGKVTIIDMV IDEKKDENQV
     TQIKLLMDVN MACLNGKERN EEEWKKLFIE AGFQHYKISP LTGFLSLIEI YP